3ms7: Difference between revisions
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==Glycogen phosphorylase complexed with 2-chlorobenzaldehyde-4-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl) thiosemicarbazone== | ==Glycogen phosphorylase complexed with 2-chlorobenzaldehyde-4-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl) thiosemicarbazone== | ||
<StructureSection load='3ms7' size='340' side='right' caption='[[3ms7]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='3ms7' size='340' side='right'caption='[[3ms7]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ms7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ms7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MS7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=22S:N-({(2E)-2-[(2-CHLOROPHENYL)METHYLIDENE]HYDRAZINO}CARBONOTHIOYL)-BETA-D-GLUCOPYRANOSYLAMINE'>22S</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ms7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ms7 OCA], [https://pdbe.org/3ms7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ms7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ms7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ms7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3ms7" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Glycogen | *[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Alexacou K-M]] | |||
[[Category: Alexacou | |||